Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

4.0K
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
4.0K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

7.1K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
7.1K
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

28.3K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
28.3K
Protein Complex Assembly02:41

Protein Complex Assembly

17.1K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
17.1K
Protein Complex Assembly02:41

Protein Complex Assembly

2.7K
2.7K
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

3.8K
The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin...
3.8K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

FCHO controls AP2's initiating role in endocytosis through a PtdIns(4,5)P<sub>2</sub>-dependent switch.

Science advances·2022
Same author

Ernst Joachim Ungewickell: 1950-2020.

The Journal of cell biology·2020
Same author

A nanobody-based molecular toolkit provides new mechanistic insight into clathrin-coat initiation.

eLife·2019
Same author

Cellular and viral peptides bind multiple sites on the N-terminal domain of clathrin.

Traffic (Copenhagen, Denmark)·2016
Same author

Transient Fcho1/2⋅Eps15/R⋅AP-2 Nanoclusters Prime the AP-2 Clathrin Adaptor for Cargo Binding.

Developmental cell·2016
Same author

A clathrin coat assembly role for the muniscin protein central linker revealed by TALEN-mediated gene editing.

eLife·2014

Related Experiment Video

Updated: Mar 28, 2026

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
08:47

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells

Published on: May 1, 2020

3.4K

F-BAR/EFC Domain Proteins: Some Assembly Required.

Linton M Traub1

  • 1Department of Cell Biology, University of Pittsburgh School of Medicine, 3500 Terrace Street, Pittsburgh, PA 15261, USA.

Developmental Cell
|December 26, 2015
PubMed
Summary
This summary is machine-generated.

BAR-domain proteins may not form polymeric spirals to sculpt cellular membranes as widely believed. This study questions the prevailing model of membrane tubulation and remodeling.

More Related Videos

FtsZ Polymerization Assays: Simple Protocols and Considerations
12:04

FtsZ Polymerization Assays: Simple Protocols and Considerations

Published on: November 16, 2013

15.9K
Bimolecular Fluorescence Complementation
08:54

Bimolecular Fluorescence Complementation

Published on: April 15, 2011

28.8K

Related Experiment Videos

Last Updated: Mar 28, 2026

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
08:47

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells

Published on: May 1, 2020

3.4K
FtsZ Polymerization Assays: Simple Protocols and Considerations
12:04

FtsZ Polymerization Assays: Simple Protocols and Considerations

Published on: November 16, 2013

15.9K
Bimolecular Fluorescence Complementation
08:54

Bimolecular Fluorescence Complementation

Published on: April 15, 2011

28.8K

Area of Science:

  • Cell Biology
  • Membrane Biology
  • Protein Biochemistry

Background:

  • BAR-domain superfamily proteins are widely thought to form polymeric spirals.
  • These structures are proposed to remodel eukaryotic phospholipid bilayers into tubules.
  • This mechanism is considered crucial for cellular trafficking and membrane dynamics.

Purpose of the Study:

  • To critically evaluate the prevailing model of BAR-domain proteins forming polymeric spirals for membrane sculpting.
  • To investigate the actual mechanism by which BAR-domain proteins influence membrane tubulation.
  • To determine if the current understanding of BAR-domain protein function in membrane remodeling is overhyped.

Main Methods:

  • Analysis of existing literature and experimental data on BAR-domain protein function.
  • In silico modeling and simulation of protein-membrane interactions.
  • Comparative studies of different BAR-domain proteins and their membrane remodeling capabilities.

Main Results:

  • Evidence suggests that BAR-domain proteins may not consistently form ordered polymeric spirals.
  • Alternative mechanisms for membrane tubulation and remodeling by BAR-domain proteins are proposed.
  • The 'overhyped' view questions the universality of the spiral model across all BAR-domain proteins.

Conclusions:

  • The widely accepted model of BAR-domain proteins forming polymeric spirals for membrane sculpting requires re-evaluation.
  • The precise mechanisms of BAR-domain mediated membrane remodeling may be more diverse than previously assumed.
  • Further research is needed to elucidate the complex roles of BAR-domain proteins in cellular membrane dynamics.